Linked Life Data

8841108

Source:http://linkedlifedata.com/resource/pubmed/id/8841108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
1996-11-12
pubmed:abstractText
Brownian dynamics simulations were performed to investigate a possible role for electrostatic channeling in transferring substrate between two of the enzymes of the citric acid cycle. The diffusion of oxaloacetate from one of the active sites of malate dehydrogenase (MDH) to the active sites of citrate synthase (CS) was simulated in the presence and absence of electrostatic forces using a modeled structure for a MDH-CS fusion protein. In the absence of electrostatic forces, fewer than 1% of substrate molecules leaving the MDH active site are transferred to CS. When electrostatic forces are present at zero ionic strength however, around 45% of substrate molecules are successfully channeled. As expected for an electrostatic mechanism of transfer, increasing the ionic strength in the simulations reduces the calculated transfer efficiency. Even at 150 mM however, the inclusion of electrostatic forces results in an increase in transfer efficiency of more than 1 order of magnitude. The simulations therefore provide evidence for the involvement of electrostatic channeling in guiding substrate transfer between two of the enzymes of the citric acid cycle. Similar effects may operate between other members of the citric acid metabolon.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12652-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Evidence for electrostatic channeling in a fusion protein of malate dehydrogenase and citrate synthase.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla 92093-0365, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't